6533b7d2fe1ef96bd125f683

RESEARCH PRODUCT

Thermal Denaturation of Pea Globulins (Pisum sativum L.)—Molecular Interactions Leading to Heat-Induced Protein Aggregation

Rémi SaurelAli AssifaouiNicolas SokJean-luc Mession

subject

Thermal denaturationProtein DenaturationHot TemperatureChromatographyCalorimetry Differential ScanningbiologyGlobulinProtein ConformationChemistryPeasfood and beveragesGlobulinsGeneral ChemistryProtein aggregationbiology.organism_classificationPisumSativumDifferential scanning calorimetrybiology.proteinLeguminElectrophoresis Polyacrylamide GelDenaturation (biochemistry)General Agricultural and Biological SciencesPlant Proteins

description

The heat-induced denaturation and aggregation of mixed pea globulins (8%, w/w) were investigated using differential scanning calorimetry (DSC), SDS-PAGE, and size-exclusion chromatography (SEC-HPLC). DSC data showed that the pea proteins denaturation temperature (T(d)) was heating-rate dependent. The T(d) value decreased by about 4 °C by lowering the heating rate from 10 to 5 °C/min. The SDS-PAGE analysis revealed that protein denaturation upon heating at 90 °C was mainly governed by noncovalent interaction. The SEC-HPLC measurements indicated that low-denatured legumin (≈350-410 kDa) and vicilin/convicilin (≈170 kDa) globulins were heat-denatured and most of their subunits reassociated into high-molecular weight, soluble aggregates (700 kDa). The addition of N-ethylmaleimide slightly modified the aggregation route of pea globulins. However, partially insoluble macroaggregates were produced in the presence of dithiothreitol, reflecting the stabilizing effect of disulfide bonds within legumin subunits.

yearjournalcountryeditionlanguage
2013-01-10Journal of Agricultural and Food Chemistry
https://doi.org/10.1021/jf303739n